The Open Protein Structure Annotation Network
PDB Keyword


    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title NMR Structure Determination of the Hypothetical Protein TM1290 from Thermotoga Maritima using Automated NOESY Analysis. J.Biomol.NMR 29 403-406 2004
    Site JCSG
    PDB Id 1rdu Target Id 283154
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1276,TM1290, 89473 Molecular Weight 12537.39 Da.
    Residues 116 Isoelectric Point 4.86
    Sequence marvaipsvgkdlssmvsdrfaraeyfiiydtesgnvevventiadahgtgpkvvqslvskgveylias nvgrnafetlkaagvkvyrfeggtvqeaidafsegrleelttftreg
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Access denied for user 'root'@'localhost' (using password: YES) (click for details)

    Ligand Information


    Google Scholar output for 1rdu
    1. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
    2. Letter to the Editor: NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis
    T Etezady-Esfarjani, T Herrmann, W Peti - Journal of biomolecular , 2004 - Springer
    3. NMR structure of the protein NP_247299. 1: comparison with the crystal structure
    K Jaudzems, M Geralt, P Serrano - Section F: Structural , 2010 - scripts.iucr.org
    4. Recognizing protein folds by cluster distance geometry
    GM Crippen - Proteins: Structure, Function, and Bioinformatics, 2005 - Wiley Online Library
    5. Evaluating the solution from MrBUMP and BALBES
    RM Keegan, F Long, VJ Fazio, MD Winn - Section D: Biological , 2011 - scripts.iucr.org
    6. Dimensionality reduction in computational demarcation of protein tertiary structures
    RR Joshi, PR Panigrahi, RN Patil - Journal of Molecular Modeling, 2011 - Springer
    7. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
    8. Crystallization and crystallographic analysis of the apo form of the orange protein (ORP) from Desulfovibrio gigas
    S Najmudin, C Bonifacio, AG Duarte - Section F: Structural , 2009 - scripts.iucr.org
    9. The Anaerobe-Specific Orange Protein Complex of Desulfovibrio vulgaris Hildenborough Is Encoded by Two Divergent Operons Coregulated by _54 and a Cognate
    A Fivet, E Cascales, M Ansaldi, SR Pauleta - Journal of , 2011 - Am Soc Microbiol

    Protein Summary

    The gene TM1290 from Thermotoga maritima encodes protein belonging to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme (dinitrogenase iron-molybdenum cofactor PF02579). This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB).  NifB appears to be an iron-sulphur source for FeMo-co biosynthesis, while NifX may be associated with the mature FeMo-co, in particular with the addition of homocitrate during the last step of biosynthesis [Ref]. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea).


    This is one of several proteins from this family ( 1o13 (T. maritima ortholog TM1816), 2re2, 2kla) solved by JCSG.

    Ligand Summary





    1. (No Results)


      Discuss this publication
    Tag page

    Files (0)

    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch